Purification and Some Properties of Two Proteinase Inhibitors (DE-1 and DE-3) fromErythrina latissima(Broad-Leaved Erythrina) Seed

Abstract

Two proteinase inhibitors, DE-1 and DE-3, were purified horn Erythrina latissima seeds. Whereas DE-1 inhibits bovine chymotrypsin and not bovine trypsin, DE-3 inhibits trypsin but not chymotrypsin. The molecular weights and the amino acid compositions of the two inhibitors resemble the corresponding properties of the Kunitz-type proteinase inhibitors. The TV-terminal primary structure of DE-3 showed homology with soybean trypsin inhibitor (Kunitz) and also with the proteinase inhibitors (A-II and B-II) homAlbizziafulibrissin seed. Reinigung und einige Eigenschaften von zwei Proteinase-Inhibitoren (DE-1 und DE-3) aus den Samen von Erythrina latissimaZusammenfassung: Zwei Proteinaseinhibitoren, DE-1 und DE-3, wurden aus den Samen von Erythrina latissima gereinigt. DE-1 inhibiert Rinderchymotrypsin und nicht Rindertrypsin, dagegen inhibiert DE-3 Trypsin, aber nicht Chymotrypsin. Die Molekulargewichte und die Aminosäurenzusammensetzungen stimmen mit den entsprechenden Eigenschaften der Proteinaseinhibitoren vom Kunitz-Typ überein. Die TV-terminale Primärstruktur von DE-3 ist homolog den Sequenzen des Sojabohnen-Trypsininhibitors (Kunitz) und den Proteinaseinhibitoren (A-II und B-II) von A Ib izzia-ju librissin-Samen.

Proteinase inhibitors and their function in plants: A review

“…Individual isoforms may differ considerably in their effects on the enzymes. For example, the seed of Erythrina latissima L. contain two inhibitors, one of which (DE-1) acts on chymotrypsin, but not trypsin, whereas the other (DE-3) is a specific trypsin inhibitor [54]. A similar picture is observed in asparagus pea [50,55] and honey locust ( Gleditsia tricanthos L.) [56,57].…”

Amino Acid Sequence of Chymotrypsin Inhibitor ECI from the Seeds ofErythrina variegata(LINN.) var.Orientalis

“…Several Kunitz-type proteinase inhibitors from the seeds of Sourthern Africa species of Erythrina have been isolated and characterized in terms of their specificities to the enzymes. 1,2) Based on their relative abilities to inhibit enzymes, they were divided into three groups: group a includes inhibitors that are relatively specific for chymotrypsin, group b includes inhibitors that inhibit trypsin strongly and chymotrypsin slightly less effectively, and group c includes inhibitors that inhibit trypsin, chymotrypsin, and t-PA as well. Thus, a characteristic feature of the Erythrina inhibitors is that unlike other leguminous proteinase inhibitors, such as soybean3) and winged bean 4 ) trypsin inhibitors, one of the trypsin inhibitors included in group c inhibits not only trypsin but also t-PA.5) Hence, biochemical studies on the Erythrina proteinase inhibitors have been focused mainly on t-PA inhibitor.…”

Effects of Mucuna pruriens Protease Inhibitors on Echis carinatus Venom

“…The gpMuc fraction from M. pruriens appeared as seven isoforms on 2D‐E, with molecular weights and p l s ranging from 20.3 to 28.7 kDa and 4.8 to 6.5 respectively. Kunitz‐type proteinase inhibitors vary in their specificity and affinity for trypsin and chymotrypsin (Joubert et al ., ; Broze et al ., ). In this experiment, the activities of trypsin and chymotrypsin were inhibited by MPE, TPE and gpMuc.…”